Advertisement

Alterations in Purine Metabolism in Cultured Fibroblasts with HGPRT Deficiency and with PRPP Synthetase Superactivity

  • Esther Zoref-Shani
  • Oded Sperling
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 122B)

Abstract

Within the last decade, two different inborn enzyme abnormalities were identified as causing excessive purine production in man: deficiency of hypoxanthine-guanine phosphoribosyltransferase(HGPRT) whether partial (1) or complete (2), and superactivity of 5-phospho-ribosyl-1-pyrophosphate (PRPP)synthetase, due to feedback-resistance (3–5) or various other molecular alterations. The finding of excessive de novo purine nucleotide synthesis in these enzyme abnormalities has contributed markedly to the understanding of the normal metabolism of purines in man, mainly in revealing the importance of HGPRT activity and of PRPP availability in the regulation of de novo purine synthesis.

Keywords

Guanine Nucleotide Purine Metabolism Nucleotide Synthesis Purine Synthesis Purine Derivative 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Kelley, W.N., Greene, M.L., Rosenbloom, F.M., Henderson, J.F. and Seegmiller, J.E. (1969). Ann. Intern. Med. 70, 155–206.Google Scholar
  2. 2.
    Seegmiller, J.E., Rosenbloom, F.M. and Kelley, W.N. (1967) Science 155, 1682–1684.PubMedCrossRefGoogle Scholar
  3. 3.
    Sperling, O., Boer, P., Persky-Brosh, S., Kanarek, E. and de Vries, A. (1972). Europ. J. Clin. Biol. Res. 17, 703–706.Google Scholar
  4. 4.
    Sperling, O., Persky-Brosh, S., Boer, P. and de Vries, A. (1973). Biochem. Med. 7, 389–395.PubMedCrossRefGoogle Scholar
  5. 5.
    Zoref, E., de Vries, A. and Sperling, O. (1975) J. Clin. Invest. 56, 1093–1099.Google Scholar
  6. 6.
    Becker, M.A., Meyer, L.J., Wood, A.W. and Seegmiller, J.E. (1973). Science (Wash. D.C.) 179, 1123–1126.Google Scholar
  7. 7.
    Becker, M.A., Meyer, L.J., Kostel, P.J. and Seegmiller, J.E. (1974). J. Clin. Invest. 53 4a.Google Scholar
  8. 8.
    Sperling, O., Frank, M., Ophir, R., Liberman, U.A., Adam, A. and de Vries, A. (1970). Europ. J. Clin. and Biol. Res. 15, 942–947.Google Scholar
  9. 9.
    Bashkin, P., Sperling, O., Schmidt, R. and Szeinberg, A. (1973) Israel J. Med. Sciences 9, 1553–1558.Google Scholar
  10. 10.
    Zoref-Shani, E., Sivan, O. and Sperling, O. (1978). BBA 521, 452–458.CrossRefGoogle Scholar
  11. 11.
    Kelley, W.N. (1968) Fed. Proc. 27, 1047–1052.PubMedGoogle Scholar
  12. 12.
    Hershfield, M.S., Spector, E.B. and Seegmiller, J.E. (1977) Adv. Exp. Med. Biol. 76A, 303–313.Google Scholar
  13. 13.
    Zoref-Shani, E. and Sperling, O. in preparation.Google Scholar
  14. 14.
    Raivio, K.O. and Seegmiller, J.E. (1973) Biochim. Biophys. Acta 299, 273–282.Google Scholar
  15. 15.
    Brox, I.W. and Henderson, J.F. (1976). Can. J. Biochem. 54, 200–202.PubMedCrossRefGoogle Scholar
  16. 16.
    Hershfield, M.S. and Seegmiller, J.E. (1977) J. Biol. Chem. 252, 6002–6010.Google Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Esther Zoref-Shani
    • 1
    • 2
  • Oded Sperling
    • 1
    • 2
  1. 1.Department of Chemical PathologyTel-Aviv University Medical SchoolTel-ShashomerIsrael
  2. 2.Beilinson Medical CenterRogoff-Wellcome Medical Research InstitutePetah-TikvaIsrael

Personalised recommendations